4rc6: Difference between revisions
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==Crystal structure of cyanobacterial aldehyde-deformylating oxygenase 122F mutant== | ==Crystal structure of cyanobacterial aldehyde-deformylating oxygenase 122F mutant== | ||
<StructureSection load='4rc6' size='340' side='right'caption='[[4rc6]]' scene=''> | <StructureSection load='4rc6' size='340' side='right'caption='[[4rc6]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RC6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rc6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RC6 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rc6 OCA], [https://pdbe.org/4rc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rc6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rc6 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rc6 OCA], [https://pdbe.org/4rc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rc6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rc6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ALDEC_SYNE7 ALDEC_SYNE7] Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.[HAMAP-Rule:MF_00931]<ref>PMID:20671186</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The fatty alk(a/e)ne biosynthesis pathway found in cyanobacteria gained tremendous attention in recent years as a promising alternative approach for biofuel production. Cyanobacterial aldehyde-deformylating oxygenase (cADO), which catalyzes the conversion of Cn fatty aldehyde to its corresponding Cn-1 alk(a/e)ne, is a key enzyme in that pathway. Due to its low activity, alk(a/e)ne production by cADO is an inefficient process. Previous biochemical and structural investigations of cADO have provided some information on its catalytic reaction. However, the details of its catalytic processes remain unclear. Here we report five crystal structures of cADO from the Synechococcus elongates strain PCC7942 in both its iron-free and iron-bound forms, representing different states during its catalytic process. Structural comparisons and functional enzyme assays indicate that Glu144, one of the iron-coordinating residues, plays a vital role in the catalytic reaction of cADO. Moreover, the helix where Glu144 resides exhibits two distinct conformations that correlates with the different binding states of the di-iron center in cADO structures. Therefore, our results provide a structural explanation for the highly labile feature of cADO di-iron center, which we proposed to be related to its low enzymatic activity. On the basis of our structural and biochemical data, a possible catalytic process of cADO was proposed, which could aid the design of cADO with improved activity. | |||
Structural insights into the catalytic mechanism of aldehyde-deformylating oxygenases.,Jia C, Li M, Li J, Zhang J, Zhang H, Cao P, Pan X, Lu X, Chang W Protein Cell. 2014 Dec 9. PMID:25482408<ref>PMID:25482408</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4rc6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] | |||
[[Category: Cao P]] | [[Category: Cao P]] | ||
[[Category: Chang WR]] | [[Category: Chang WR]] | ||
Latest revision as of 18:14, 8 November 2023
Crystal structure of cyanobacterial aldehyde-deformylating oxygenase 122F mutantCrystal structure of cyanobacterial aldehyde-deformylating oxygenase 122F mutant
Structural highlights
FunctionALDEC_SYNE7 Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.[HAMAP-Rule:MF_00931][1] Publication Abstract from PubMedThe fatty alk(a/e)ne biosynthesis pathway found in cyanobacteria gained tremendous attention in recent years as a promising alternative approach for biofuel production. Cyanobacterial aldehyde-deformylating oxygenase (cADO), which catalyzes the conversion of Cn fatty aldehyde to its corresponding Cn-1 alk(a/e)ne, is a key enzyme in that pathway. Due to its low activity, alk(a/e)ne production by cADO is an inefficient process. Previous biochemical and structural investigations of cADO have provided some information on its catalytic reaction. However, the details of its catalytic processes remain unclear. Here we report five crystal structures of cADO from the Synechococcus elongates strain PCC7942 in both its iron-free and iron-bound forms, representing different states during its catalytic process. Structural comparisons and functional enzyme assays indicate that Glu144, one of the iron-coordinating residues, plays a vital role in the catalytic reaction of cADO. Moreover, the helix where Glu144 resides exhibits two distinct conformations that correlates with the different binding states of the di-iron center in cADO structures. Therefore, our results provide a structural explanation for the highly labile feature of cADO di-iron center, which we proposed to be related to its low enzymatic activity. On the basis of our structural and biochemical data, a possible catalytic process of cADO was proposed, which could aid the design of cADO with improved activity. Structural insights into the catalytic mechanism of aldehyde-deformylating oxygenases.,Jia C, Li M, Li J, Zhang J, Zhang H, Cao P, Pan X, Lu X, Chang W Protein Cell. 2014 Dec 9. PMID:25482408[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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